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Title: All in the Packaging: Structural and Electronic Effects of Nanoconfinement on Metal Oxide Nanoparticles

Abstract

Encapsulation of inorganic nanoparticles within oligomeric protein cages can provide a multivalent approach for the synthesis of biocompatible nanomaterials by combining the nanoparticle-forming catalytic abilities of the cage interior with the biointeractive exterior surface of the cage. Protein cages provide more than simply a passive compartment for nanoparticle formation: protein-templated nanoparticles can exhibit structural and electronic properties that are dramatically different from materials synthesized without protein templating. Mixed Fe/Mn oxides formed under hydrothermal conditions form a structural series ranging from the {gamma}-Fe{sub 2}O{sub 3} (maghemite) to the Mn{sub 3}O{sub 4} (hausmannite) spinel structure as the Mn fraction is increased from 0 to 100%, while similar materials formed inside of human ferritin transition instead from maghemite to a layered Mn oxide structure similar to chalcophanite. The electronic properties of the protein-templated nanoparticles, as determined from soft X-ray absorption spectroscopy, also differ from those of their protein-free counterparts, in agreement with the structural results. Protein-templated synthesis may provide the opportunity for powerful control over nanomaterial properties through nanoconfinement, but the ultimate physical basis for these effects remains to be determined.

Authors:
; ; ;  [1]
  1. (Montana)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFDOE - BASIC ENERGY SCIENCESNASA
OSTI Identifier:
1024048
Resource Type:
Journal Article
Journal Name:
Chem. Mater.
Additional Journal Information:
Journal Volume: 23; Journal Issue: (17) ; 09, 2011; Journal ID: ISSN 0897-4756
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ABSORPTION SPECTROSCOPY; COMPARTMENTS; COMPOSITE MATERIALS; DISTRIBUTION FUNCTIONS; ENCAPSULATION; FERRITES; FERRITIN; OXIDES; PACKAGING; PROTEINS; SPINELS; SYNTHESIS; X-RAY SPECTROSCOPY

Citation Formats

Jolley, Craig, Pool, Vanessa, Idzerda, Yves, and Douglas, Trevor. All in the Packaging: Structural and Electronic Effects of Nanoconfinement on Metal Oxide Nanoparticles. United States: N. p., 2011. Web. doi:10.1021/cm201295p.
Jolley, Craig, Pool, Vanessa, Idzerda, Yves, & Douglas, Trevor. All in the Packaging: Structural and Electronic Effects of Nanoconfinement on Metal Oxide Nanoparticles. United States. doi:10.1021/cm201295p.
Jolley, Craig, Pool, Vanessa, Idzerda, Yves, and Douglas, Trevor. Tue . "All in the Packaging: Structural and Electronic Effects of Nanoconfinement on Metal Oxide Nanoparticles". United States. doi:10.1021/cm201295p.
@article{osti_1024048,
title = {All in the Packaging: Structural and Electronic Effects of Nanoconfinement on Metal Oxide Nanoparticles},
author = {Jolley, Craig and Pool, Vanessa and Idzerda, Yves and Douglas, Trevor},
abstractNote = {Encapsulation of inorganic nanoparticles within oligomeric protein cages can provide a multivalent approach for the synthesis of biocompatible nanomaterials by combining the nanoparticle-forming catalytic abilities of the cage interior with the biointeractive exterior surface of the cage. Protein cages provide more than simply a passive compartment for nanoparticle formation: protein-templated nanoparticles can exhibit structural and electronic properties that are dramatically different from materials synthesized without protein templating. Mixed Fe/Mn oxides formed under hydrothermal conditions form a structural series ranging from the {gamma}-Fe{sub 2}O{sub 3} (maghemite) to the Mn{sub 3}O{sub 4} (hausmannite) spinel structure as the Mn fraction is increased from 0 to 100%, while similar materials formed inside of human ferritin transition instead from maghemite to a layered Mn oxide structure similar to chalcophanite. The electronic properties of the protein-templated nanoparticles, as determined from soft X-ray absorption spectroscopy, also differ from those of their protein-free counterparts, in agreement with the structural results. Protein-templated synthesis may provide the opportunity for powerful control over nanomaterial properties through nanoconfinement, but the ultimate physical basis for these effects remains to be determined.},
doi = {10.1021/cm201295p},
journal = {Chem. Mater.},
issn = {0897-4756},
number = (17) ; 09, 2011,
volume = 23,
place = {United States},
year = {2011},
month = {9}
}